Experts and Doctors on glycerol kinase in College Station, Texas, United States

Summary

Locale: College Station, Texas, United States
Topic: glycerol kinase

Top Publications

  1. Yu P, Lasagna M, Pawlyk A, Reinhart G, Pettigrew D. IIAGlc inhibition of glycerol kinase: a communications network tunes protein motions at the allosteric site. Biochemistry. 2007;46:12355-65 pubmed
    ..Steady-state and time-resolved fluorescence anisotropy measurements show that the motions of the fluorophore reflect backbone motions of the IIAGlc-binding site and these motions are modulated by the amino acids at the coupling locus. ..
  2. Pettigrew D, Ma D, Conrad C, Johnson J. Escherichia coli glycerol kinase. Cloning and sequencing of the glpK gene and the primary structure of the enzyme. J Biol Chem. 1988;263:135-9 pubmed
    ..Examination of the upstream DNA sequence reveals two possible promoters of essentially the same efficiency: the P1 promoter of pBR322 and a hybrid promoter which contains both bacterial and pBR322 DNA sequences. ..
  3. Holtman C, Pawlyk A, Meadow N, Pettigrew D. Reverse genetics of Escherichia coli glycerol kinase allosteric regulation and glucose control of glycerol utilization in vivo. J Bacteriol. 2001;183:3336-44 pubmed
  4. Holtman C, Pawlyk A, Meadow N, Roseman S, Pettigrew D. IIA(Glc) allosteric control of Escherichia coli glycerol kinase: binding site cooperative transitions and cation-promoted association by Zinc(II). Biochemistry. 2001;40:14302-8 pubmed
    ..The similarity of effects of the alanine substitutions of the amino acids in the alpha-helical region for IIA(Glc) binding affinity and cation-promoted association by Zn(II) indicates that they function as a cooperative unit. ..
  5. Yu P, Pettigrew D. Linkage between fructose 1,6-bisphosphate binding and the dimer-tetramer equilibrium of Escherichia coli glycerol kinase: critical behavior arising from change of ligand stoichiometry. Biochemistry. 2003;42:4243-52 pubmed
    ..5) is due to the approximately 4000-fold higher affinity of the tetramer for FBP rather than to positive coupling between the two FBP sites. ..
  6. Pettigrew D. Amino acid substitutions in the sugar kinase/hsp70/actin superfamily conserved ATPase core of E. coli glycerol kinase modulate allosteric ligand affinity but do not alter allosteric coupling. Arch Biochem Biophys. 2009;481:151-6 pubmed publisher
    ..These possibilities may arise from differences of E. coli glycerol kinase relative to other superfamily members with respect to oligomeric structure and location of the allosteric site in a single domain far from the catalytic site. ..
  7. Pettigrew D. Oligomeric interactions provide alternatives to direct steric modes of control of sugar kinase/actin/hsp70 superfamily functions by heterotropic allosteric effectors: inhibition of E. coli glycerol kinase. Arch Biochem Biophys. 2009;492:29-39 pubmed publisher
    ..The oligomeric interactions enable the heterotropic allosteric effectors to act on both domains and modulate the catalytic cleft closure despite binding to only one domain. ..
  8. Pettigrew D, Yu G, Liu Y. Nucleotide regulation of Escherichia coli glycerol kinase: initial-velocity and substrate binding studies. Biochemistry. 1990;29:8620-7 pubmed
    ..Several properties of the enzyme are consistent with negative cooperativity as the basis for the difference in affinities. The possible physiological importance of the regulatory behavior with respect to ATP is considered. ..
  9. Pettigrew D, Liu W, Holmes C, Meadow N, Roseman S. A single amino acid change in Escherichia coli glycerol kinase abolishes glucose control of glycerol utilization in vivo. J Bacteriol. 1996;178:2846-52 pubmed

More Information

Publications11

  1. Holtman C, Thurlkill R, Pettigrew D. Unexpected presence of defective glpR alleles in various strains of Escherichia coli. J Bacteriol. 2001;183:1459-61 pubmed
    ..Analysis of the effects on growth and enzyme expression show that glucose repression of glycerol utilization is not dependent on a functional repressor. ..
  2. Pawlyk A, Pettigrew D. Transplanting allosteric control of enzyme activity by protein-protein interactions: coupling a regulatory site to the conserved catalytic core. Proc Natl Acad Sci U S A. 2002;99:11115-20 pubmed